Q71XX5 (MURE_LISMF) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 57.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase EC=6.3.2.13 Alternative name(s): Meso-A2pm-adding enzyme Meso-diaminopimelate-adding enzyme UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase UDP-MurNAc-tripeptide synthetase UDP-N-acetylmuramyl-tripeptide synthetase | ||||
| Gene names |
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| Organism | Listeria monocytogenes serotype 4b (strain F2365) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 265669 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria |
Protein attributes
| Sequence length | 491 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan By similarity. HAMAP MF_00208 |
| Catalytic activity | ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate. HAMAP MF_00208 |
| Pathway | Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00208. |
| Post-translational modification | Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP MF_00208 |
| Sequence similarities | Belongs to the MurCDEF family. MurE subfamily. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 491 | 491 | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208 | PRO_0000101910 | |||||
Regions | |||||||||
| Nucleotide binding | 108 – 114 | 7 | ATP Potential | ||||||
| Region | 150 – 151 | 2 | UDP-MurNAc-L-Ala-D-Glu binding By similarity | ||||||
| Region | 407 – 410 | 4 | Meso-diaminopimelate binding By similarity | ||||||
| Motif | 407 – 410 | 4 | Meso-diaminopimelate recognition motif HAMAP MF_00208 | ||||||
Sites | |||||||||
| Binding site | 30 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 149 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 177 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 183 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 185 | 1 | UDP-MurNAc-L-Ala-D-Glu By similarity | ||||||
| Binding site | 383 | 1 | Meso-diaminopimelate By similarity | ||||||
| Binding site | 458 | 1 | Meso-diaminopimelate; via carbonyl oxygen By similarity | ||||||
| Binding site | 462 | 1 | Meso-diaminopimelate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 217 | 1 | N6-carboxylysine By similarity | ||||||
Sequences
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References
| [1] | "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species." Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., Daugherty S.C., Dodson R.J. Fraser C.M.Nucleic Acids Res. 32:2386-2395(2004) [PubMed: 15115801] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: F2365. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017262 Genomic DNA. Translation: AAT04840.1. |
| RefSeq | YP_014663.1. NC_002973.6. |
3D structure databases | |
| ProteinModelPortal | Q71XX5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q71XX5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2797029. |
| GenomeReviews | Gene locus LMOf2365_2070 in contig AE017262_GR. |
| KEGG | lmf:LMOf2365_2070. |
| PATRIC | 20325435. VBILisMon105049_2077. |
| TIGR | LMOf2365_2070. |
Phylogenomic databases | |
| eggNOG | COG0769. |
| HOGENOM | HBG602753. |
| OMA | SCANAAG. |
| PhylomeDB | Q71XX5. |
| ProtClustDB | PRK00139. |
Enzyme and pathway databases | |
| BioCyc | LMON265669:LMOF2365_2070-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00208. MurE. [Tree] |
| InterPro | IPR018109. Folylpolyglutamate_synth_CS. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view] |
| Gene3D | G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit. |
| KO | K01928. |
| Pfam | PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view] |
| SUPFAM | SSF53244. Mur_ligase_C. 1 hit. SSF53623. Mur_ligase_cen. 1 hit. |
| TIGRFAMs | TIGR01085. MurE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MURE_LISMF | ||||||||
| Accession | Primary (citable) accession number: Q71XX5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with